9IJO

X-ray crystal structure of F46C myoglobin with a covalently linked 4-methyl-2,2'-bipyridine group in complex with Cu2+

This is a non-PDB format compatible entry.

Summary for 9IJO

• Entry DOI: 10.2210/pdb9ijo/pdb
• Descriptor: Myoglobin, PROTOPORPHYRIN IX CONTAINING FE, 4-methyl-2-(4-methylpyridin-2-yl)pyridine, ... (5 entities in total)
• Functional Keywords: heme protein, myoglobin, copper binding, metal binding protein
• Biological source: Physeter catodon (sperm whale)
• Total number of polymer chains: 1
• Total formula weight: 18186.39

Authors

Lin, Y.W. (deposition date: 2024-06-25, release date: 2025-07-02, Last modification date: 2026-07-15)

Primary citation

Nie, L.S.,Liu, X.C.,Yu, L.,Liu, A.K.,Sun, L.J.,Gao, S.Q.,Lin, Y.W.
Rational Design of an Artificial Metalloenzyme by Constructing a Metal-Binding Site Close to the Heme Cofactor in Myoglobin.
Inorg.Chem., 63:18531-18535, 2024

PubMed Abstract: In this study, we constructed a metal-binding site close to the heme cofactor in myoglobin (Mb) by covalently attaching a nonnative metal-binding ligand of bipyridine to Cys46 through the F46C mutation in the heme distal site. The X-ray structure of the designed enzyme, termed F46C-mBpy Mb, was solved in the Cu(II)-bound form, which revealed the formation of a heterodinuclear center of Cu-His-HO-heme. Cu(II)-F46C-mBpy Mb exhibits not only nitrite reductase reactivity but also cascade reaction activity involving both hydrolysis and oxidation. Furthermore, F46C-mBpy Mb displays Mn-peroxidase activity by the oxidation of Mn to Mn using HO as an oxidant. This study shows that the construction of a nonnative metal-binding site close to the heme cofactor is a convenient approach to creating an artificial metalloenzyme with a heterodinuclear center that confers multiple functions.

PubMed: 39311200
DOI: 10.1021/acs.inorgchem.4c03093

Experimental method

X-RAY DIFFRACTION (1.53 Å)